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  • Biochemistry and Biotechnology  (2,788)
  • Deutschland
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  • 1985-1989  (2,792)
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Year
  • 11
    Electronic Resource
    Electronic Resource
    A standard formula for the determination of the initial rate of hydrolysis of carboxymethylcellulose (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 409-414 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The integrated rate equation of Huang, originally used to describe the hydrolysis of insoluble acid treated cellulose, is shown equally applicable in describing the hydrolysis of carboxymethylcellulose (CMC) using a dilution series of Cellulomonas sp. ATCC 21399 crude cellulase as enzyme preparation. Interpretation of the progress curves of hydrolysis of CMC according to the integrated rate equation is used to calculate a standard formula for the conversion of the rate of hydrolysis into the initial velocity of hydrolysis. The validity of the standard formula is tested, using enzyme preparations from Cellulomonas grown under varied conditions, and enzyme preparations containing purified endoglucanases from Cellulomonas.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270404
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  • 12
    Electronic Resource
    Electronic Resource
    Studies on chemically aggregated pepsin using glutaraldehyde (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 415-419 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Porcine pepsin was immobilized by chemical aggregation using glutaraldehyde as a bifunctional crosslinking agent. The immobilzed pepsin followed Michaelis-Menten kinetics (Km = 5.3 × 10-5 M) and the yield of immobilization was 91%. The activation energy of the immobilized preparation was 90,613 cal/mol as compared to 67,532 cal/mol for native pepsin. Using acid-denatured hemoglobin and N-acetyl phenyl-alanyl-3, 5-diiodotyrosine (APDT) as substrates, the activities shown by the immobilized pepsin were, respectively, 67 and 79% that of the soluble pepsin. The immobiized pepsin showed marked stabilization against pH, temperature, urea, and guanidine hydrochloride. The activity of the immobilized preparation in the presence of urea was greater when hemoglobin was used as the substrate than when APDT was used as substrate. Storage of the preparation under refrigerated conditions for 160 days showed 58% retention in enzyme activity. The immobilized pepsin can be removed from the reaction mixture volume easily, retaining nearly 100% of its activity even after being used in seven consecutive assays.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270405
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  • 13
    Electronic Resource
    Electronic Resource
    The response of a nitrogen-limited chemostat culture of Escherichia coli B/r to pH and dilution rate steps (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 439-446 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of four pH steps and one dilution rate step are described for an ammonia-nitrogen-limited continuous culture of Escherichia coli B/r. Two of the pH steps, 6.06-5.49 and 5.96-5.60, led to prolonged transients in both cell density and rate-limiting nutrient concentration. The other two pH steps, 6.20-5.96 and 5.60-6.20, had almost no effect on the culture. The dilution rate step led to a sharp transition in the steady-state external pyruvate concentration. Monitoring of the external pyruvate concentration for the pH 5.96-5.60 step revealed that the transient phase continued long after the cell density and rate-limiting nutrient concentration returned to steady-state values. The implications for industrial and laboratory fermentations are discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270408
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  • 14
    Electronic Resource
    Electronic Resource
    Purification and immobilization of rabbit liver aldehyde oxidasePart 14 in “The use of enzymes in organic synthesis.” For part 13 see M. C. R. Franssen and H. C. van der Plas, Recl. Trav. Chim. Pays-Bas., 103, 99 (1984). (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 447-455 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aldehyde oxidase (E.C. 1.2.3.1) was isolated from rabbit liver and two potential bioaffinity ligands, i.e., 3-aminocarbonyl-1-benzyl-6-methylpyridinium bromide and 3-aminocarbonyl-1-benzyl-4,6-dimethylpyridinium chloride, were tested for their applicability in a purification procedure for this enzyme. Various supports and different coupling methods were investigated for the immobilization of aldehyde oxidase. Adsorption to n-hexyl- and n-octylamine-substituted Sepharose 4B and DEAE Sepharose 6B gave the best retention of aldehyde oxidase activity. The storage stability of free enzyme and enzyme immobilized to n-octylamine-substituted Sepharose 4B was studied in several buffers at pH 7.8 and 9.0. This showed that the stability of immobilized enzyme was much less than that of free enzyme. The apparent operational stability of the immobilized enzyme preparation, however, improved substantially compared to soluble enzyme, although the corresponding product yield is still very poor. Coimmobilization of catalase and/or superoxide dismutase provided no significant increase of the apparent operational stability and product yield. A positive effect on both parameters was found for aldehyde oxidase-n-alkylamine Sepharose 4B preparations by increasing the amount of enzyme adsorbed per unit weight of support, whereas the productivity of these preparations remained about constant.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270409
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  • 15
    Electronic Resource
    Electronic Resource
    Kinetics of cellobiose hydrolysis using cellobiase composites from Ttrichoderma reesei and Aspergillus niger (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 463-470 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The enzymatic hydrolysis of cellulose to glucose involves the formation of cellobiose as an intermediate. It has been found necessary1 to add cellobiase from Aspergillus niger (NOVO) to the cellobiase component of Trichoderma reesei mutant Rut C-30 (Natick) cellulase enzymes in order to obtain after 48 h complete conversion of the cellobiose formed in the enzymatic hydrolysis of biomass. This study of the cellobiase activity of these two enzyme sources was undertaken as a first step in the formation of a kinetic model for cellulose hydrolysis that can be used in process design. In order to cover the full range of cellobiose concentrations, it was necessary to develop separate kinetic parameters for high- and low-concentration ranges of cellobiose for the enzymes from each organism. Competitive glucose inhibition was observed with the enzymes from both organisms. Substrate inhibition was observed only with the A. niger enzymes.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270411
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  • 16
    Electronic Resource
    Electronic Resource
    Oxygen transfer in liquids (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 503-508 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In the laboratory-type airlift tower reactor oxygen transfer from air in tap water and/or polyacrylamide solutions (Neuperm WF) was studied. In order to characterize the system, volumetric coefficient of oxygen transfer was determined by the gassing-out method. Two arrangements of the airlift tower reactor were compared, namely the reactor with and without motionless mixer. In addition, mean relative gas holdup and gas power output were determined for both arrangements.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270416
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  • 17
    Electronic Resource
    Electronic Resource
    Performance of hydrophobic chromatography in purification of α-amylase (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 514-518 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Hydrophobic ligands were introduced onto agarose beads, and the adsorption capacity of the beads was measured. The adsorption capacity increased with increase in the carbon number of the ligand, ionic strength of the buffer solution, and temperature. Crude α-amylase was purified with these hydrophobic adsorbents and the breakthrough and elution curves were estimated based on the mass transfer theory. Under strongly hydrophobic conditions, impurities contained in crude feeds and the lack of uniformity of packing caused by aggregation of beads affected adsorption and elution behaviors.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270418
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  • 18
    Electronic Resource
    Electronic Resource
    Chemical and enzymic pretreatment of corn stover to produce soluble fermentation substrates (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 362-368 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Corn stover was pretreated with various chemical agents, including sodium hydroxide, sulfuric acid, ethylenediamine, n-butylamine (either alone or in solution with methanol), and acetonitrile or ethanol containing hydrochloric acid. Of these chemicals, n-butylamine was the best reagent for pretreatment of corn stover, considering the degree of loss of total carbohydrate, delignification, cumulative weight loss, cumulative yield of reducing sugars per original total carbohydrate, and the potential ease of recovery and reuse of reagent. In comparison to the other reagents tested, n-butylamine (n-BA) selectively delignified corn stover. The best conditions were as follows: a 12-h presoak of about a 155 g dry wt/L slurry (1 mm average particle size) in 100% n-BA at room temperature, followed by 30 min of refluxing (86.5°C) with 40% (w/w) n-BA-distilled water solution. The cumulative yield of reducing sugars after enzymic hydrolysis was 44.5% of the original total carbohydrate and the cumulative total weight loss (dry basis) was 59%. Degradative loss of total carbohydrate during pretreatment was not detected.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270322
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  • 19
    Electronic Resource
    Electronic Resource
    Simultaneous saccharification and fermentation of cellulose: Effect of ethanol on enzymatic saccharification of cellulose (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 389-397 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: It was confirmed that simultaneous saccharification and fermentation are effective for accelerating enzymatic saccharification of cellulose. In this work, the effects of ethanol on the saccharification of tissue paper by Trichoderma cellulase (Meicelase CEPB) have been investigated. The following results were obtained. (1) Saccharification was inhibited by at least 0.2M ethanol. (2) Less than 4M ethanol did not affect the enzymatic activities of β-glucosidase and endoglucanase (Cx) at all. The thermal stability of endoglucanase was not also varied by ethanol. (3) It is suggested that ethanol depresses the adsorption of exoglucanase on cellulose. (4) The rate expression of saccharification of cellulose in the presense of ethanol is proposed. (5) The inhibititory effect of ethanol was found to become more significant in the later stages of the reaction than just the initial stage.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270402
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  • 20
    Electronic Resource
    Electronic Resource
    Immobilization of a soluble chemically thermostabilized enzyme (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 572-578 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cellobiase was coupled to a dialdehyde dextran by reductive alkylation in the presence of sodium cyanoborohydride. The resulting conjugate, obtained without loss of enzymic activity, presents properties of thermoresistance largely superior to those of native enzyme: the rate of inactivation is reduced compared to that of native enzyme and its optimal temperature of activity is 70-75°C instead of 65°C. Finally the conjugate presents increased longevity when subjected to experiments of operational stability; its hydrolytic activity is maintained at 60°C in a 10% (w/v) cellobiose solution for more than 100 h whereas the native enzyme is inactivated after 45 h. The cellobiase-dextran conjugate was immobilized by covalent coupling on aminated silica by reductive alkylation in the presence of NaBH3CN. The characteristics of thermoresistance of this stabilized and immobilized conjugate were studied and compared to those of a preparation of native cellobiase immobilized on a silica support activated with glutaraldehyde. Analysis of the thermoresistance of these two cellobiase preparations clearly shows that immobilization has maintained and even enhanced their properties. In particular, the operational stability, measured at 68°C on 10% (w/v) cellobiose shows an increased longevity of the stabilized and immobilized enzyme for 120 h compared to 60 h for the native immobilized enzyme. Two successive incubations of these cellobiase derivatives show that it is possible to obtain 2.5 times more glucose with the stabilized-immobilized enzyme than with the immobilized preparation. The procedure described above enables us to prepare a thermostabilized immobilized cellobiase.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270505
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